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Thiol-disulfide oxidoreductase LTO1 (EC 1.1.4.-) (Protein LUMEN THIOL OXIDOREDUCTASE 1) (Vitamin K reductase)

 LTO1_ARATH              Reviewed;         376 AA.
Q8L540; O81807; Q8L9V9;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-APR-2018, entry version 105.
RecName: Full=Thiol-disulfide oxidoreductase LTO1 {ECO:0000303|PubMed:22209765};
EC=1.1.4.- {ECO:0000305};
AltName: Full=Protein LUMEN THIOL OXIDOREDUCTASE 1 {ECO:0000303|PubMed:22209765};
AltName: Full=Vitamin K reductase {ECO:0000303|PubMed:20626653};
Flags: Precursor;
Name=LTO1 {ECO:0000303|PubMed:22209765};
Synonyms=VKOR {ECO:0000303|PubMed:20626653};
OrderedLocusNames=At4g35760 {ECO:0000312|Araport:AT4G35760};
ORFNames=F8D20.270 {ECO:0000312|EMBL:CAA20046.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20626653; DOI=10.1111/j.1365-313X.2010.04305.x;
Furt F., Van Oostende C., Widhalm J.R., Dale M.A., Wertz J.,
Basset G.J.;
"A bimodular oxidoreductase mediates the specific reduction of
phylloquinone (vitamin K(1)) in chloroplasts.";
Plant J. 64:38-46(2010).
[6]
FUNCTION, INTERACTION WITH PSBO1 AND PSBO2, TOPOLOGY, AND DISRUPTION
PHENOTYPE.
PubMed=22209765; DOI=10.1105/tpc.111.089680;
Karamoko M., Cline S., Redding K., Ruiz N., Hamel P.P.;
"Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is
required for the assembly of photosystem II in Arabidopsis.";
Plant Cell 23:4462-4475(2011).
[7]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-46;
CYS-109; CYS-116; CYS-195; CYS-198; CYS-230; CYS-293; CYS-296; CYS-316
AND CYS-331.
PubMed=21781282; DOI=10.1111/j.1742-4658.2011.08265.x;
Feng W.K., Wang L., Lu Y., Wang X.Y.;
"A protein oxidase catalysing disulfide bond formation is localized to
the chloroplast thylakoids.";
FEBS J. 278:3419-3430(2011).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23689258; DOI=10.1007/s00299-013-1455-9;
Lu Y., Wang H.R., Li H., Cui H.R., Feng Y.G., Wang X.Y.;
"A chloroplast membrane protein LTO1/AtVKOR involving in redox
regulation and ROS homeostasis.";
Plant Cell Rep. 32:1427-1440(2013).
[9]
FUNCTION, AND INTERACTION WITH TL20.3; HCF164; PETJ; VDE1; EDA3; TL17;
FKBP13 AND FKBP20-2.
PubMed=25412899;
Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
"Identification of potential targets for thylakoid oxidoreductase
AtVKOR/LTO1 in chloroplasts.";
Protein Pept. Lett. 22:219-225(2014).
-!- FUNCTION: Thiol-disulfide oxidoreductase catalyzing disulfide bond
formation of chloroplast proteins and involved in redox regulation
and photosynthetic electron transport. Required for the assembly
of photosystem II (PSII) through the formation of disulfide bond
in PSBO, a subunit of the PSII oxygen-evolving complex in the
thylakoid lumen. Involved in the formation of disulfide bonds in
the lumenal protein FKBP13. In vitro, reduces phylloquinone
(vitamin K1) and menaquinone (vitamin K2) to their respective
quinol. Cannot reduce phylloquinone epoxide to phylloquinone
(PubMed:20626653, PubMed:21781282, PubMed:22209765,
PubMed:23689258). Plays an important role in regulating the
thylakoid lumen redox (PubMed:25412899).
{ECO:0000269|PubMed:20626653, ECO:0000269|PubMed:21781282,
ECO:0000269|PubMed:22209765, ECO:0000269|PubMed:23689258,
ECO:0000269|PubMed:25412899}.
-!- SUBUNIT: Interacts with the PSII subunits PSBO1 and PSBO2
(PubMed:22209765). Interacts with TL17, TL20.3, HCF164, PETJ,
VDE1, EDA3, FKBP13 and FKBP20-2 (PubMed:25412899).
{ECO:0000269|PubMed:22209765, ECO:0000269|PubMed:25412899}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000305|PubMed:20626653, ECO:0000305|PubMed:21781282}; Multi-
pass membrane protein {ECO:0000305|PubMed:20626653,
ECO:0000305|PubMed:21781282}.
-!- TISSUE SPECIFICITY: Expressed in cotyledons, rosette leaves,
stems, cauline leaves and flowers. {ECO:0000269|PubMed:20626653}.
-!- DOMAIN: Cysteine residues from the thioredoxin-like domain
participate in a series of disulfide-exchange reactions that
regenerate the redox-active cysteine residues in the transmembrane
domain. {ECO:0000250|UniProtKB:Q2JJF6}.
-!- DISRUPTION PHENOTYPE: Severe growth defects due to a limitation in
the electron flow from PSII. {ECO:0000269|PubMed:22209765,
ECO:0000269|PubMed:23689258}.
-!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM65737.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA20046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB81485.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL031135; CAA20046.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161588; CAB81485.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86559.1; -; Genomic_DNA.
EMBL; AY099728; AAM20579.1; -; mRNA.
EMBL; AY128903; AAM91303.1; -; mRNA.
EMBL; AY088194; AAM65737.1; ALT_INIT; mRNA.
PIR; T04681; T04681.
RefSeq; NP_567988.1; NM_119742.4.
UniGene; At.43284; -.
ProteinModelPortal; Q8L540; -.
SMR; Q8L540; -.
BioGrid; 15011; 10.
IntAct; Q8L540; 1.
MINT; Q8L540; -.
STRING; 3702.AT4G35760.1; -.
PaxDb; Q8L540; -.
EnsemblPlants; AT4G35760.1; AT4G35760.1; AT4G35760.
GeneID; 829729; -.
Gramene; AT4G35760.1; AT4G35760.1; AT4G35760.
KEGG; ath:AT4G35760; -.
Araport; AT4G35760; -.
TAIR; locus:2128028; AT4G35760.
eggNOG; ENOG410IENU; Eukaryota.
eggNOG; COG4243; LUCA.
HOGENOM; HOG000232446; -.
InParanoid; Q8L540; -.
OMA; WCPHCHE; -.
OrthoDB; EOG09360F3A; -.
PhylomeDB; Q8L540; -.
PRO; PR:Q8L540; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q8L540; baseline and differential.
Genevisible; Q8L540; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:TAIR.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
Gene3D; 1.20.1440.130; -; 1.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR012932; VKOR.
InterPro; IPR038354; VKOR_sf.
Pfam; PF07884; VKOR; 1.
SMART; SM00756; VKc; 1.
SUPFAM; SSF52833; SSF52833; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Disulfide bond; Membrane;
Oxidoreductase; Plastid; Quinone; Redox-active center;
Reference proteome; Thylakoid; Transit peptide; Transmembrane;
Transmembrane helix.
TRANSIT 1 45 Chloroplast. {ECO:0000255}.
CHAIN 46 376 Thiol-disulfide oxidoreductase LTO1.
/FTId=PRO_0000428663.
TOPO_DOM 46 81 Stromal. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TOPO_DOM 103 125 Lumenal. {ECO:0000255}.
TRANSMEM 126 146 Helical. {ECO:0000255}.
TOPO_DOM 147 165 Stromal. {ECO:0000255}.
TRANSMEM 166 186 Helical. {ECO:0000255}.
TOPO_DOM 187 192 Lumenal. {ECO:0000255}.
TRANSMEM 193 213 Helical. {ECO:0000255}.
TOPO_DOM 214 223 Stromal. {ECO:0000255}.
TRANSMEM 224 244 Helical. {ECO:0000255}.
TOPO_DOM 245 376 Lumenal. {ECO:0000255}.
COMPBIAS 47 78 Ser-rich.
DISULFID 109 116 Redox-active. {ECO:0000255}.
DISULFID 195 198 Redox-active.
{ECO:0000250|UniProtKB:Q2JJF6}.
DISULFID 293 296 Redox-active. {ECO:0000255}.
DISULFID 316 331 Redox-active. {ECO:0000255}.
MUTAGEN 46 46 C->A: No effect on catalysis of disulfide
bond. {ECO:0000269|PubMed:21781282}.
MUTAGEN 109 109 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 116 116 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 195 195 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 198 198 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 230 230 C->A: No effect on catalysis of disulfide
bond. {ECO:0000269|PubMed:21781282}.
MUTAGEN 293 293 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 296 296 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 316 316 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
MUTAGEN 331 331 C->A: Loss of function in catalyzing
disulfide bond.
{ECO:0000269|PubMed:21781282}.
SEQUENCE 376 AA; 40401 MW; 21D60947ADCB6D95 CRC64;
MMARFVSVSS CQFHFGFREV SPPSVTSYPR RFEVSDRRFP AIPIKCSSSE PENGEDSAPS
LSSSSSSSTS EVSTSNSSTY NWYTGIGGIG MLDTAYLTYL KVTGSDAFCP IGGGTCGDVL
NSDYAVVFGV PLPVIGFVMY GVVTALSAEL GEGNLPFGIS KSNGRFALFG ITTAMASASA
YFLYILSTKL SGSSCLYCLV SAFLSFSLFF LSVKDVKLQE IQQVVGLQIC LAIIVVASLT
ASYSTAQPIP SRSGDIELPY FRTEISSSSS PYAIALAKHL NSIGAKMYGA FWCSHCLEQK
EMFGREAAKE LNYVECFPDG YKKGTKILKA CADAAIEGFP TWIINDKVLS GEIELAELAE
MTGFSLDQAN ETNQLQ


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